Recombinant Protein Production with Prokaryotic and Eukaryotic Cells. A Comparative View on Host Physiology: Selected articles from the Meeting of the EFB Section on Microbial Physiology, Semmering, Austria, 5th–8th October 2000 PDF
Preview Recombinant Protein Production with Prokaryotic and Eukaryotic Cells. A Comparative View on Host Physiology: Selected articles from the Meeting of the EFB Section on Microbial Physiology, Semmering, Austria, 5th–8th October 2000
RECOMBINANT PROTEIN PRODUCTION WITH PROKARYOTIC AND EUKARYOTIC CELLS. A COMPARATIVE VIEW ON HOST PHYSIOLOGY RECOMBINANT PROTEIN PRODUCTION WITH PROKARYOTIC AND EUKARYOTIC CELLS. A COMPARATIVE VIEW ON HOST PHYSIOLOGY Selected artic1es from the Meeting of the EFB Seetion on Microbial Physiology, Semmering, Austria, 5th-8th October 2000 Edited by 0.-W. MERTEN Genethon IlI, Evry-Cedex, France D. MATTANOVICH University of Agricultural Sciences, Institute for Applied Microbiology, Wien, Austria C. LANG Technical University of Berlin, Institute of Biotechnology, Berlin, Germany G. LARSSON KTH, The Swedish Centre on Bioprocess Technology, Stockholm, Sweden P. NEUBAUER M. Luther University of Halle-Wittenberg, Institute of Biotechnology, Halle, Germany D. PORRO Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan. Italy P. POSTMA E.c. Slater Institute, University ofA msterdam, The Netherlands J. TEIXEIRA DE MATTOS Swammerdam Institute of Life Sciences, University ofA msterdam, The Netherlands J.A. COLE School of Biosciences, University of Birmingham, United Kingdom Springer-Science+Business Media, B.V. Library of Congress Cataloging-in-Publication Data Recombinant protein production with prokaryotic and eukaryotic cells : a comparative view on host physiology : selected articles from the meeting of the EFB Section on Microbial Physiology, SemmeringlA, 5th-8th October 2000 / edited by O.-W. Merten ... [et al.]. p.em. Inc1udes index. 1. Industrial microbiology. 2. Recombinant microorganisms. 3. Recombinant proteins. I. Merten, O.-W. II. European Federation ofBiotechnology. Section on Microbial Physiology. QR53 .R425 2001 660.6'2--dc21 2001038619 ISBN 978-90-481-5756-3 ISBN 978-94-015-9749-4 (eBook) DOI 10.1007/978-94-015-9749-4 Printed on acid-free paper All Rights Reserved © 2001 Springer Science+Business Media Dordrecht Originally published by Kluwer Academic Publishers in 2001. Softcover reprint ofthe hardcover 1st edition 2001 No part of the material protected by this copyright notice may be reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording or by any information storage and retrieval system, without written permission from the copyright owner. TABLE OF CONTENTS Foreword IX Cell-free translation systems Pro tein synthesis and co-translational folding in cell-free translation systems Spirin, A.S. 1 Metabolie burden and stress response The cellular response to unfolded proteins in the endoplasmic reticulum Kaufman, R., Scheuner, D., Tirasophon, W., Yin-Liu, C., Song, B., Lee, K.C., McEwen, E., Weir, S.-B. 17 The effects of recombinant protein expression on the growth and metabolism of mammalian cells Yallop, C.A., Svendsen, 1. 29 Mapping stresses in Escherichia cali to improve yield. Examining global gene regulation and « cell conditioning » strategies DeLisa, M.P., Gill, R.T., Bentley, W.E. 43 Cellular responses to strong overexpression of recombinant genes in Escherichia cali. DNA relaxation and cell death after induction of (X glucosidase Lin, H.Y., Hanschke, R., Nicklisch, S., Nietsehe, T., Jarchow, R., Schwahn, c., Riemschneider, S., Meyer, S., Gupta, A., Hecker, M., Neubauer, P. 55 From Vitreascilla hemoglobin (VHb) to a novel class of growth stimulating hemoglobin proteins Kallio, P.T., Frey, A.D., Bailey, J.E. 75 Genetie stability and gene eopy number effeets Protein mass production in hybridomas and recombinant CHO cells vi T ABLE OF CONTENTS Kunert, R., Strutzenberger, K., Steindl, F., Zudjelovic, A., Borth, N., Katinger, H. 89 Inducible gene copy number amplification for the production of heterologous pro teins in Kluyveromyces lactis Bianchi, M.M. 99 Antibiotic-free plasmid selection and maintenance in Bacteria Hanak, J.A.J., Cranenburgh, R.M. 111 Modelling of segregational plasmid instability of recombinant strain suspension of Escherichia coli Boudrant, J., Le, B.-L., Foumier, F., Fonteix, C. 125 Transcription, translation, and product formation in E. coli Production of optically pure aryl epoxides by recombinant E. coli carrying styrene monooxgenase. A new biocatalyst based on pseudomonas fluorescens ST genes Colmegna, A., SeHo, G., Galli, E., Bestetti, G. 141 Translational problems associated with the rare arginine CGG in Escherichia coli . Frameshifting at eGG codons McNulty, D.E., Huddleston, M.J., Claffee, B., Green, S., Sathe, G., Reeves, R., Patel, P., Kane, J.F. 151 Optimisation ofthe solubility ofthe recombinant Itk kinase domain in Escherichia coli Meinander, N., Jeppsson, M., Sögaard, M. 159 Bacterial senescence and the oxidation paradox Nyström, T., BaHesteros, M., Fredriksson, A. 171 Metabolie approaehes for the optimisation of reeombinant fermentation proeesses Striedner, G., Cserjan-Pusehmann, M., Grabherr, R., Clementsehitsch, F., Nilsson, E., Bayer, K. 179 T ABLE OF CONTENTS vii Control and optimisation of eellular bottleneeks in reeombinant protein produetion Sanden, A.M., Larsson, G. 189 Expression and fermentation strategies for reeombinant pro tein produetion in Escherichia coli. Neubauer, P., Winter, J. 195 Transcription, translation, and product formation in microbial systems other than E. coli Overexpression of a Rhizopus oryzae lipase in Pichia pastoris strains eontaining multiple eopies of the target gene Serrano, A., Cereghino, G.L., Ferrer, P., Cregg, J.M., Valero, F. 259 Development of a heterologous gene expression system for use in Lactococcus lactis. A novel gram-positive expression system Bredmose, L., Madsen, S.M., Vrang, A., Ravn, P., Johnsen, M.G., Glenting, J., Amau, J., Israelsen, H. 269 Metabolie network analysis for human therapeutie protein produetions : effects of the P/O ratio Calik, P., Özdamar, T.H. 277 Animal cell based expression systems - process optimisation Process-orientated metabolic engineering: cell lines with new properties in nutrient exploitation and protein glycosylation Wagner, R. 289 Influenee of the metabolie status of paekaging eells on retroviral veetor produetion Merten, O.-W., Landrie, L., Danos, O. 303 Optimizing the produetion ofreeombinant prion pro tein from CHO cells Bocking, S.P., Steane, S.E., Saini, S., Bennett, A.D. 319 V1 11 T ABLE OF CONTENTS Recombinant protein production by transient transfection of suspension-growing cells Durocher, Y., PeITet, S., Kamen, A. 331 Comparison of different microbial expression systems Production of recombinant human trypsinogen in Eseheriehia eoli and Piehia pastoris. A comparison of expression systems Hohenblum, H., Naschberger, S., Weik, R., Katinger, H., Mattanovich D. 339 Secretion ofhomologous and heterologous recombinant proteins in Eseherichia coli and other gram-negative bacteria by using a new secretion system Miksch, G., Flaschel, E. 347 Monitoring of genes that respond to overproduction of insoluble recombinant proteins in Escherichia coli and Bacillus subtilis Schweder, T., Jürgen, B. 359 Model supported optimization of fed-batch fermentations for recombinant protein production Volk, N., Franco-Lara, E., Galvanauskas, V., Lübbert, A. 371 Protease secretion capacity and performance analysis of recombinant Bacillus species Calik, P., Kalender, N., Özdamar, T.H. 383 Subject Index 393 Authors Index 399 Foreword More then 20 years have passed now since the first recombinant protein producing microorganisms have been developed. In the meanwhile, numerous proteins have been produced in bacteria, yeasts and filamentous fungi, as weIl as higher eukaryotic cells, and even entire plants and animals. Many recombinant proteins are on the market today, and some of them reached substantial market volumes. On the first sight one would expect the technology - including the physiology of the host strains - to be optimised in detail after a 20 year's period of development. However, several constraints have limited the incentive for optimisation, especially in the pharmaceutical industry like the urge to proceed quickly or the requirement to define the production parameters for registration early in the development phase. The additional expenses for registration of a new production strain often prohibits a change to an optimised strain. A continuous optimisation of the entire production process is not feasible for the same reasons. To define the status of the physiological research on recombinant protein producing organisms and to identify trends towards generally applicable solutions for physiological constraints, the Section on Microbial Physiology of the European Federation of Biotechnology organised a conference entitled "Recombinant Protein Production with Prokaryotic and Eukaryotic Host Cells. A Comparative View on Host Physiology" in Semmering, Austria, in 2000. The organisation was supported by: Institute of Applied Microbiology (lAM) at the University of Agricultural Sciences Vienna; European Society for Animal Cell Technology (ESACT); Austrian Society for Biotechnology (ÖGBT); Verein Österreichischer Lebensmittel- und Biotechnologen (VÖLB); and Österreichische Gesellschaft für Hygiene, Mikrobiologie und Präventivmedizin (ÖGHMP). A special feature of this meeting was the comparison of different classes of host cells, mainly bacteria, yeasts, filamentous fungi and animal cells, which made obvious that many physiological features of recombinant protein formation, like cell nutrition, stress responses, protein folding and secretion, or genetic stability follow similar patterns in different expression systems. Due to the success of this meeting it was decided to update the most important informations, and to make them available to a wider community in the form of this volume. The volume beg ins (certainly achallenge for all microbiologists) with a detailed description of cell-free protein synthesis. This technique, brought to maturity in Prof. Spirin 's lab in the last decades, is able today to replace recombinant gene expression in a significant number of applications. The following chapter concentrates on stress responses to recombinant protein formation ranging from mammalian cells to bacteria. Then, genetic stability and gene copy number effects ix x are treated from copy number effects in mammalian cells and yeasts to modelling as weil as maintenance of plasmid stability in E. caU. Transcription, translation and product formation in E. cali: treats mainly the identification of bottlenecks in the production of different proteins and approaches to circumvent them, whereas in other microbial systems like non-conventional yeasts and gram-positive bacteria the principle physiological characteristics are still not weil defined. To round up the informations on animal cells given before, aspects of process optimisation are treated from the engineering of cell lines to the production of proteins by transient transfection. Finally several studies compare different microbial expression systems with the aim to define guidelines for the choice between host organisms. It can be concluded that a close co-operation between process development and strain improvement is crucial for the optimisation of both the production strain and the process, and can be very rewarding especially for products with lower unit value. In the ne ar future, microbial physiology will playamajor role to define and generalise the physiological principles and constraints for recombinant protein production. In order to speed up the development of new products, more comparative data between different host organisms, aimed to define solid guidelines for the choice of the best production vehicle, are urgently needed. Vienna, May 2001 The editors
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